메뉴 건너뛰기




Volumn 43, Issue 31, 2004, Pages 10058-10063

Alanine-scanning mutagenesis in the signature disulfide loop of the glycine receptor α1 subunit: Critical residues for activation and modulation

Author keywords

[No Author keywords available]

Indexed keywords

ANESTHETICS; ELECTRIC CURRENTS; HYDROPHOBICITY; IONS; MODULATION; SURFACE PROPERTIES; TRANSCEIVERS;

EID: 3543083927     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036159g     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 0001202076 scopus 로고
    • Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer
    • Langosch, D., Thomas, L., and Betz, H. (1988) Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer, Proc. Natl. Acad. Sci. U.S.A. 85, 7394-7398.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 2
    • 0030780210 scopus 로고    scopus 로고
    • Prediction of the secondary structure of the nicotinic acetylcholine receptor nontransmembrane regions
    • Ortells, M. O. (1997) Prediction of the secondary structure of the nicotinic acetylcholine receptor nontransmembrane regions, Proteins 29, 391-398.
    • (1997) Proteins , vol.29 , pp. 391-398
    • Ortells, M.O.1
  • 3
    • 0036286167 scopus 로고    scopus 로고
    • NMR structures of the second transmembrane domain of the human glycine receptor α(1) subunit: Model of pore architecture and channel gating
    • Tang, P., Mandal, P. K., and Xu, Y. (2002) NMR structures of the second transmembrane domain of the human glycine receptor α(1) subunit: Model of pore architecture and channel gating, Biophys. J. 83, 252-262.
    • (2002) Biophys. J. , vol.83 , pp. 252-262
    • Tang, P.1    Mandal, P.K.2    Xu, Y.3
  • 4
    • 0026787189 scopus 로고
    • Distinct agonist- and antagonist-binding sites on the glycine receptor
    • Vandenberg, R. J., Handford, C. A., and Schofield, P. R. (1992) Distinct agonist- and antagonist-binding sites on the glycine receptor, Neuron 9, 491-496.
    • (1992) Neuron , vol.9 , pp. 491-496
    • Vandenberg, R.J.1    Handford, C.A.2    Schofield, P.R.3
  • 5
    • 0027224010 scopus 로고
    • Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers
    • Bormann, J., Rundstrom, N., Betz, H., and Langosch, D. (1993) Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers, EMBO J. 12, 3729-3737.
    • (1993) EMBO J. , vol.12 , pp. 3729-3737
    • Bormann, J.1    Rundstrom, N.2    Betz, H.3    Langosch, D.4
  • 6
    • 0344172759 scopus 로고    scopus 로고
    • Molecular determinants of glycine receptor subunit assembly
    • Griffon, N., Buttner, C., Nicke, A., Kuhse, J., Schmalzing, G., and Betz, H. (1999) Molecular determinants of glycine receptor subunit assembly, EMBO J. 18, 4711-4721.
    • (1999) EMBO J. , vol.18 , pp. 4711-4721
    • Griffon, N.1    Buttner, C.2    Nicke, A.3    Kuhse, J.4    Schmalzing, G.5    Betz, H.6
  • 8
    • 0037021325 scopus 로고    scopus 로고
    • The inhibitory glycine receptor-simple views of a complicated channel
    • Breitinger, H. G., and Becker, C. M. (2002) The inhibitory glycine receptor-simple views of a complicated channel, ChemBioChem 3, 1042-1052.
    • (2002) ChemBioChem , vol.3 , pp. 1042-1052
    • Breitinger, H.G.1    Becker, C.M.2
  • 9
    • 0036842245 scopus 로고    scopus 로고
    • Modulation of glycine receptor function: A novel approach for therapeutic intervention at inhibitory synapses?
    • Laube, B., Maksay, G., Schemm, R., and Betz, H. (2002) Modulation of glycine receptor function: A novel approach for therapeutic intervention at inhibitory synapses? Trends Pharmacol. Sci. 23, 519-527.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 519-527
    • Laube, B.1    Maksay, G.2    Schemm, R.3    Betz, H.4
  • 11
    • 0027282161 scopus 로고
    • Positive modulation of human γ-aminobutyric acid type A and glycine receptors by the inhalation anesthetic isoflurane
    • Harrison, N. L., Kugler, J. L., Jones, M. V., Greenblatt, E. P., and Pritchett, D. B. (1993) Positive modulation of human γ-aminobutyric acid type A and glycine receptors by the inhalation anesthetic isoflurane, Mol. Pharmacol. 44, 628-632.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 628-632
    • Harrison, N.L.1    Kugler, J.L.2    Jones, M.V.3    Greenblatt, E.P.4    Pritchett, D.B.5
  • 13
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Fujiyoshi, Y., and Unwin, N. (2003) Structure and gating mechanism of the acetylcholine receptor pore, Nature 424, 949-955.
    • (2003) Nature , vol.424 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 14
    • 0034255021 scopus 로고    scopus 로고
    • Specific binding sites for alcohols and anesthetics on ligand-gated ion channels
    • Mascia, M. P., Trudell, J. R., and Harris, R. A. (2000) Specific binding sites for alcohols and anesthetics on ligand-gated ion channels. Proc. Natl. Acad. Sci. U.S.A. 97, 9305-9310.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9305-9310
    • Mascia, M.P.1    Trudell, J.R.2    Harris, R.A.3
  • 15
    • 0141483292 scopus 로고    scopus 로고
    • A highly conserved aspartic acid residue in the signature disulfide loop of the α1 subunit is a determinant of gating in the glycine receptor
    • Schofield, C. M., Jenkins, A., and Harrison, N. L. (2003) A highly conserved aspartic acid residue in the signature disulfide loop of the α1 subunit is a determinant of gating in the glycine receptor, J. Biol. Chem. 278, 34079-34083.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34079-34083
    • Schofield, C.M.1    Jenkins, A.2    Harrison, N.L.3
  • 16
    • 0037448581 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in the GABA(A) receptor
    • Kash, T. L., Jenkins, A., Kelley, J. C., Trudell, J. R., and Harrison, N. L. (2003) Coupling of agonist binding to channel gating in the GABA(A) receptor, Nature 421, 272-275.
    • (2003) Nature , vol.421 , pp. 272-275
    • Kash, T.L.1    Jenkins, A.2    Kelley, J.C.3    Trudell, J.R.4    Harrison, N.L.5
  • 17
    • 0347379903 scopus 로고    scopus 로고
    • Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor
    • Absalom, N. L., Lewis, T. M., Kaplan, W., Pierce, K. D., and Schofield, P. R. (2003) Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor, J. Biol. Chem. 278, 50151-50157.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50151-50157
    • Absalom, N.L.1    Lewis, T.M.2    Kaplan, W.3    Pierce, K.D.4    Schofield, P.R.5
  • 18
    • 0035902019 scopus 로고    scopus 로고
    • Neurobiology. Snails, synapses, and smokers
    • Dougherty, D. A., and Lester, H. A. (2001) Neurobiology. Snails, synapses, and smokers, Nature 411, 252-253, 255.
    • (2001) Nature , vol.411 , pp. 252-253
    • Dougherty, D.A.1    Lester, H.A.2
  • 19
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van Der Oost, J., Smit, A. B., and Sixma, T. K. (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors, Nature 411, 269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    Van Der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 22
    • 0036062998 scopus 로고    scopus 로고
    • Molecular modelling of specific and non-specific anaesthetic interactions
    • Trudell, J. R., and Bertaccini, E. (2002) Molecular modelling of specific and non-specific anaesthetic interactions, Br. J. Anaesth. 89, 32-40.
    • (2002) Br. J. Anaesth. , vol.89 , pp. 32-40
    • Trudell, J.R.1    Bertaccini, E.2
  • 23
    • 0036019297 scopus 로고    scopus 로고
    • Predicting the transmembrane secondary structure of ligand-gated ion channels
    • Bertaccini, E., and Trudell, J. R. (2002) Predicting the transmembrane secondary structure of ligand-gated ion channels, Protein Eng. 15, 443-454.
    • (2002) Protein Eng. , vol.15 , pp. 443-454
    • Bertaccini, E.1    Trudell, J.R.2
  • 24
    • 4143088670 scopus 로고    scopus 로고
    • Comparative modeling of a GABAA α1 receptor using three crystal structures as templates
    • Trudell, J. R., and Bertaccini, E. (2004) Comparative modeling of a GABAA α1 receptor using three crystal structures as templates, J. Mol. Graphics Modell. 23, 39-49.
    • (2004) J. Mol. Graphics Modell. , vol.23 , pp. 39-49
    • Trudell, J.R.1    Bertaccini, E.2
  • 25
    • 0029895146 scopus 로고    scopus 로고
    • Effects of inhalational general anaesthetics on native glycine receptors in rat medullary neurones and recombinant glycine receptors in Xenopus oocytes
    • Downie, D. L., Hall, A. C., Lieb, W. R., and Franks, N. P. (1996) Effects of inhalational general anaesthetics on native glycine receptors in rat medullary neurones and recombinant glycine receptors in Xenopus oocytes, Br. J. Pharmacol. 118, 493-502.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 493-502
    • Downie, D.L.1    Hall, A.C.2    Lieb, W.R.3    Franks, N.P.4
  • 26
    • 0027169801 scopus 로고
    • The extracellular disulfide loop motif of the inhibitory glycine receptor does not form the agonist binding site
    • Vandenberg, R. J., Rajendra, S., French, C. R., Barry, P. H., and Schofield, P. R. (1993) The extracellular disulfide loop motif of the inhibitory glycine receptor does not form the agonist binding site, Mol. Pharmacol. 44, 198-203.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 198-203
    • Vandenberg, R.J.1    Rajendra, S.2    French, C.R.3    Barry, P.H.4    Schofield, P.R.5
  • 27
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • Lynch, J. W., Rajendra, S., Pierce, K. D., Handford, C. A., Barry, P. H., and Schofield, P. R. (1997) Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel, EMBO J. 16, 110-120.
    • (1997) EMBO J. , vol.16 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 28
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity, and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. (1998) Binding, gating, affinity, and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors, Br. J. Pharmacol. 125, 924-947.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 29
    • 0037329589 scopus 로고    scopus 로고
    • Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating
    • Shen, X. M., Ohno, K., Tsujino, A., Brengman, J. M., Gingold, M., Sine, S. M., and Engel, A. G. (2003) Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating, J. Clin. Invest. 111, 497-505.
    • (2003) J. Clin. Invest. , vol.111 , pp. 497-505
    • Shen, X.M.1    Ohno, K.2    Tsujino, A.3    Brengman, J.M.4    Gingold, M.5    Sine, S.M.6    Engel, A.G.7
  • 31
    • 0242268392 scopus 로고    scopus 로고
    • Conformation-dependent hydrophobic photolabeling of the nicotinic receptor: Electrophysiology-coordinated photochemistry and mass spectrometry
    • Leite, J. F., Blanton, M. P., Shahgholi, M., Dougherty, D. A., and Lester, H. A. (2003) Conformation-dependent hydrophobic photolabeling of the nicotinic receptor: Electrophysiology-coordinated photochemistry and mass spectrometry, Proc. Natl. Acad. Sci. U.S.A. 100, 13054-13059.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13054-13059
    • Leite, J.F.1    Blanton, M.P.2    Shahgholi, M.3    Dougherty, D.A.4    Lester, H.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.